Detection of Species Specific Epitopes of Mouse and Hamster Prion Proteins (PrPs) by Anti-peptide Antibodies

Overview

Journal Arch Virol

Specialty Microbiology

Date 1996 Jan 1

PMID 8645112

Citations 4

Authors

T Yokoyama

S Itohara

N Yuasa

Affiliations

Soon will be listed here.

Abstract

Antisera to four synthetic peptides containing the substitutions between mouse and hamster prion proteins (PrPs) were produced in rabbits. The synthetic peptides used represent two mouse (Mo-I: residues 100-115 and Mo-V: residues 199-208) and two hamster PrP subregion sequences (Ha-I: 101-116 and Ha-V: 200-209). All antisera reacted strongly with homologous peptides but either not at all or poorly with heterologous peptides in enzymelinked immunosorbent assay (ELISA). Antisera to Mo-I and Mo-V recognized mouse PrPSc but not hamster PrpSc in western blot analysis (WB) and ELISA. Antisera to Ha-I contain antibodies specific to hamster PrPSc. The results indicate that these regions of PrPSc constitute species-specific epitopes. In contrast to these antisera, the antiserum to Ha-V recognized neither hamster nor mouse PrPSc. In this study, we identified mouse subregion-V as a species-specific epitope.

Citing Articles

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

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Characterization of Syrian hamster adapted prions derived from L-type and C-type bovine spongiform encephalopathies.

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The immunodetection of the abnormal isoform of prion protein.

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Immunoreactivity of specific epitopes of PrPSc is enhanced by pretreatment in a hydrated autoclave.

Yokoyama T, Momotani E, Kimura K, Yuasa N Clin Diagn Lab Immunol. 1996; 3(4):470-1.

PMID: 8807215 PMC: 170369. DOI: 10.1128/cdli.3.4.470-471.1996.

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